R5258
Riboflavin Binding Protein from chicken egg white
lyophilized powder
Synonym(s):
Binding Protein, Chicken Egg White Protein, Riboflavin Protein
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.26
Recommended Products
biological source
chicken egg white
form
lyophilized powder
concentration
≥50% protein (biuret)
UniProt accession no.
storage temp.
−20°C
Gene Information
chicken ... RBP(396449)
General description
Riboflavin Binding Protein (RBP) comprises of 19 cysteines and corresponds to a molecular weight of 30 kDa. Egg white RBP is produced in the oviduct cells. Chicken egg white RBP contains an N-terminal ligand binding domain and a C-terminal phosphorylated motif.
Riboflavin binding protein (RBP) transports riboflavin through the bloodstream of the laying hen into the eggs, where the vitamin is essential for embryonic growth and development. RBP consists of a single polypeptide chain containing 9 disulfide bonds. It is a glycoprotein containing ~14% carbohydrate, with sugar moieties including galactose, mannose and glucosamine, and is phosphorylated.
Application
Riboflavin Binding Protein from chicken egg white may be used in fluorescence quenching experiments.
Biochem/physiol Actions
Riboflavin Binding Protein (RBP) is crucial for normal embryo development. RBP interacts with riboflavin and its analogs. The RBP-riboflavin complex is stabilized by interaction between the isoalloxazyne ring of riboflavin and the tyrosine 75 and tryptophan 156 of residues of RBP. RBP elicits sweet supressing functionality and may interact with the sweet taste receptor.
Riboflavin binding protein binds to flavokinase and regulates its activity.
Preparation Note
Supplied as the riboflavin-depleted apo-form.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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The effect of riboflavin binding protein (RPB) on flavokinase catalytic activity.
Slomczynska, M.
Comparative Biochemistry and Physiology, 87, 681-685 (1987)
Electrochemistry of riboflavin-binding protein and its interaction with riboflavin
Bartovsik M, et al.
Bioelectrochemistry, 76(1-2), 70-75 (2009)
Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners
Maehashi K, et al.
Chemical Senses, 32(2), 183-190 (2006)
Crystal structure of chicken riboflavin-binding protein
Monaco HL
The Embo Journal, 16(7), 1475-1483 (1997)
Binding study of riboflavin-binding protein with riboflavin and its analogues by differential scanning calorimetry
Wasylewski M
Journal of Protein Chemistry, 19(6), 523-528 (2000)
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